Carbohydrate characterization of purified thyroxine-binding globulin by lectin blot and isoelectric focusing | Zendy

Ivana Petrović | Zendy; Svetlana Savin-Zegarac | Zendy; Ivona Baričević | Zendy; Dubravka Cvejić | Zendy

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Carbohydrate characterization of purified thyroxine-binding globulin by lectin blot and isoelectric focusing

Author(s) -

Ivana Petrović,

Svetlana Savin-Zegarac,

Ivona Baričević,

Dubravka Cvejić

Publication year - 2003

Publication title -

jugoslovenska medicinska biohemija

Language(s) - English

Resource type - Journals

eISSN - 1452-8193

pISSN - 0354-3447

DOI - 10.2298/jmh0304319p

Subject(s) - lectin , isoelectric focusing , agglutinin , biochemistry , wheat germ agglutinin , soybean agglutinin , sialic acid , isoelectric point , western blot , biology , microbiology and biotechnology , chemistry , enzyme , gene

Summary: The structure of carbohydrate moiety of purified thyroxine-binding globulin (TBG) was examined by lectin blot and isoelectric focusing (IEF). In lectin blot, TBG reacted positively with the following lectins: Sambucus nigra agglutinin (SNA I), Ricinus communis agglutinin (RCA I), wheat germ lectin (WGA), phytoheamagglutinin (PHA) and pea lectin (PSA). The obtained results indicate that purified TBG contains N-linked oligosaccharide chains consisting of mannose, galactose, N-acetylglucosamine and sialic acid. Isoelectric focusing of TBG at pI 4.2’ 4.6 revealed three bands, which confirmed that isolated TBG had retained its structure without desialylation. Lectin blot analysis and IEF can be considered to be useful tools in the study of TBG glycosylation.

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